Recombinant Human alpha 1 Fetoprotein
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Recombinant Human alpha 1 Fetoprotein is a Human Full Length protein, in the 19 to 609 aa range, expressed in Insect cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
HPAFP, AFP, Alpha-fetoprotein, Alpha-1-fetoprotein, Alpha-fetoglobulin
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human alpha 1 Fetoprotein (AB207113)
SDS-PAGE analysis of ab207113 (3μg) under reducing condition and visualized by coomassie blue stain.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Alpha-fetoprotein functions as a fetal plasma protein with roles similar to serum albumin including the binding and transport of ligands such as bilirubin and fatty acids. It does not form part of any larger protein complex but is significant in modulating fetal immune tolerance. In the fetal environment AFP helps protect cells from maternal immune attacks by binding to estrogens and other growth-modulating factors. Its function during pregnancy is critical for maintaining homeostasis and ensuring the fetus's viability.
Pathways
Alpha 1-fetoprotein plays a role in several important biological pathways related to cellular growth and immune response modulation. One such pathway involves regulation of cell proliferation and differentiation in the developing liver. AFP interacts with cellular receptors that influence these processes. Additionally it plays a part in immune pathways interacting with elements that control immune overlooking to fetal antigens hence being linked to both hepatic and immune system proteins like albumin and estrogen receptors.
Specifications
Form
Liquid
Additional notes
Affinity purified
General info
Function
Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.
Sequence similarities
Belongs to the ALB/AFP/VDB family.
Post-translational modifications
Independent studies suggest heterogeneity of the N-terminal sequence of the mature protein and of the cleavage site of the signal sequence.. Sulfated.
Target data
Product promise
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